628280-43-3

Usage

Uses

Used in Biochemistry and Molecular Biology:
N-Fmoc DMNB-L-serine is used as a key component in the synthesis of caged protein kinase sensors for monitoring intracellular enzymatic activity. The application reason is its unique photolytic properties, which allow for the controlled release of the serine molecule upon exposure to light, enabling the study of protein kinase activity in living cells.
Used in Pharmaceutical Research:
In the pharmaceutical industry, N-Fmoc DMNB-L-serine is used as a building block for the development of novel drug candidates targeting protein kinases. The application reason is its ability to modulate protein kinase activity, which plays a crucial role in various cellular signaling pathways and is often dysregulated in diseases such as cancer, making it an attractive therapeutic target.
Used in Drug Delivery Systems:
N-Fmoc DMNB-L-serine can also be employed in the design of drug delivery systems, particularly for the targeted delivery of protein kinase inhibitors. The application reason is its compatibility with various drug carrier platforms, such as nanoparticles and liposomes, which can enhance the bioavailability and therapeutic efficacy of the drug candidates.

Upstream product

• 1016-58-6 6-nitroveratryl alcohol 
• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 
• 628280-41-1 4,5-dimethoxy-2-nitrobenzyl trichloroacetimidate 
• 136497-85-3 N-(9-fluorenylmethoxycarbonyl)-L-serine allyl ester 
• 628280-42-2 N-(9-fluorenylmethyloxycarbonyl)-o-(4,5-dimethoxy-2-nitrobenzyl)-L-serine allyl ester 

Downstream Products

• 780009-55-4 (S)-2-Amino-3-(4,5-dimethoxy-2-nitro-benzyloxy)-propionic acid 

Relevant academic research and scientific papers

An Integrated Chemical Cytometry Method: Shining a Light on Akt Activity in Single Cells

Tools to evaluate oncogenic kinase activity in small clinical samples have the power to guide precision medicine in oncology. Existing platforms have demonstrated impressive insights into the activity of protein kinases, but these technologies are unsuitable for the study of kinase behavior in large numbers of primary human cells. To address these limitations, we developed an integrated analysis system that utilizes a light-programmable, cell-permeable reporter deliverable simultaneously to many cells. The reporter's ability to act as a substrate for Akt, a key oncogenic kinase, was masked by a 2-4,5-dimethoxy 2-nitrobenzyl (DMNB) moiety. Upon exposure to ultraviolet light and release of the masking moiety, the substrate sequence enabled programmable reaction times within the cell cytoplasm. When coupled to automated single-cell capillary electrophoresis, statistically significant numbers of primary human cells were readily evaluated for Akt activity.

Long-wavelength fluorescent reporters for monitoring protein kinase activity

In vivo optical imaging must contend with the limitations imposed by the optical window of tissue (600-1000 nm). Although a wide array of fluorophores are available that are visualized in the red and near-IR region of the spectrum, with the exception of proteases, there are few long wavelength probes for enzymes. This situation poses a particular challenge for studying the intracellular biochemistry of erythrocytes, the high hemoglobin content of which optically obscures subcellular monitoring at wavelengths less than 600 nm. To address this, tunable fluorescent reporters for protein kinase activity were developed. The probing wavelength is preprogrammed by using readily available fluorophores, thereby enabling detection within the optical window of tissue, specifically in the far-red and near-IR region. These agents were used to monitor endogenous cAMP-dependent protein kinase activity in erythrocyte lysates and in intact erythrocytes when using a light-activatable reporter. Searching far and near: Fluorescent reporters for protein kinase activity were developed. The probing wavelength is preprogrammed by using readily available fluorophores, thereby enabling detection within the optical window of tissue, specifically in the far-red and near-IR region. These agents were used to monitor endogenous cAMP-dependent protein kinase activity 1) in erythrocyte lysates and 2) in intact erythrocytes when using a light-activatable reporter.

Fluorescent assays for protein kinases

This invention provides fluorescently-labeled peptide substrates for protein kinases; methods using the substrates for identifying compounds that inhibit protein kinases, for determining if particular protein kinases are active in cells, for diagnosing di

A Light-Activated Probe of Intracellular Protein Kinase Activity

The first example of a photoactivated probe of intracellular enzymatic activity is described. The caged derivative of a fluorescent protein kinase C peptide-based sensor was prepared by modifying the free hydroxyl group of a phosphorylatable serine moiety with a photolabile appendage that blocks phosphoryl transfer. We have demonstrated that the caged sensor allows one to (1) sample PKC activity with exquisite temporal precision, (2) control the relative amount of active sensor available for phosphorylation, and (3) examine protein kinase activity at multiple time points. Copyright